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Protein

Phospholipase A2 taicatoxin

Gene
N/A
Organism
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Heterotrimer: blocks the voltage-dependent L-type calcium channels from the heart, and the small conductance calcium-activated potassium channels in the chromaffin cells and in the brain. Is very toxic to mice.
Monomer: Snake venom phospholipase A2 (PLA2) that has neurotoxic activities. Voltage-dependently affects ionic currents in chick (Gallus domesticus) dorsal root ganglion cells. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phospholipase A2 activity Source: UniProtKB-EC

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Calcium-activated potassium channel impairing toxin, Hydrolase, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase A2 taicatoxin (EC:3.1.1.4)
Short name:
TCX
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
OrganismiOxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Taxonomic identifieri8667 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeOxyuranus

Subcellular locationi

  1. Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of the monomer is 500 µg/kg to mice.
LD50 of the heterotrimer is 50-100 µg/kg to mice.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›27›27Phospholipase A2 taicatoxinPRO_0000408515Add
BLAST

Post-translational modificationi

Contains 7 disulfide bonds.By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Interactioni

Subunit structurei

Heterotrimer composed of an alpha-neurotoxin-like peptide of 8 kDa (AC P0CJ35), this neurotoxic phospholipase of 16 kDa and a serine protease inhibitor of 7 kDa (AC B7S4N9) at an approximate stoichiometry of 1:1:4; non-covalently linked.1 Publication

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR016090. PLipase_A2_dom.
[Graphical view]
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q7LZG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
NLAQFGFMIR CANGGSRSAL DYADYGC
Length:27
Mass (Da):2,901
Last modified:December 15, 2003 - v1
Checksum:iA74F18ACB843133C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei27 – 271

Sequence databases

PIRiA34280.
S21101.

Cross-referencesi

Web resourcesi

Wikipedia

Taicatoxin entry

Sequence databases

PIRiA34280.
S21101.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR016090. PLipase_A2_dom.
[Graphical view]
PfamiPF00068. Phospholip_A2_1. 1 hit.
[Graphical view]
SUPFAMiSSF48619. SSF48619. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Anionic currents of chick sensory neurons are affected by a phospholipase A2 purified from the venom of the taipan snake."
    Possani L.D., Mochca-Morales J., Amezcua J., Martin B.M., Prestipino G., Nobile M.
    Biochim. Biophys. Acta 1134:210-216(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE.
    Tissue: Venom.
  2. "Isolation and physiological characterization of taicatoxin, a complex toxin with specific effects on calcium channels."
    Possani L.D., Martin B.M., Yatani A., Mochca-Morales J., Zamudio F.Z., Gurrola G.B., Brown A.M.
    Toxicon 30:1343-1364(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE.
    Tissue: Venom.
  3. "Effect of TaiCatoxin (TCX) on the electrophysiological, mechanical and biochemical characteristics of spontaneously beating ventricular cardiomyocytes."
    Fantini E., Athias P., Tirosh R., Pinson A.
    Mol. Cell. Biochem. 160:61-66(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe."
    Doorty K.B., Bevan S., Wadsworth J.D.F., Strong P.N.
    J. Biol. Chem. 272:19925-19930(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Taicatoxin inhibits the calcium-dependent slow motility of mammalian outer hair cells."
    Su M.-C., Lee S.-Y., Tan C.-T., Su C.-C., Li S.-Y., Lin R.-H., Hung C.-C., Lin M.-J.
    Hear. Res. 203:172-179(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPA2T_OXYSC
AccessioniPrimary (citable) accession number: Q7LZG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: December 15, 2003
Last modified: January 7, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.